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Immobilization of a novel cold active esterase onto Fe3O4∼cellulose nano-composite enhances catalytic properties.

Abstract：

:A novel esterase, EstH was cloned, purified and characterized from the marine bacterium Zunongwangia sp. The purified EstH showed optimum activity at 30°C and pH 8.5 with ∼50% of original activity at 0°C. EstH was stable in high salt conditions (0-4.5M NaCl). To improve the characteristics and explore the possibilities for application, a new immobilization matrix, Fe3O4∼cellulose nano-composite, was prepared and was characterized by Fourier Transform Infrared Spectroscopy (FTIR) and Scanning Electron Microscope (SEM). Interestingly the optimal temperature of immobilized EstH elevated to 35°C. Compared to its free form, immobilized EstH showed better temperature stability (48.5% compared to 22.40% at 50°C after 30min), prolonged half-life (32h compared to 18h), higher storage stability (∼71% activity compared to ∼40% after 50days of storage), improved pH tolerance (∼73% activity at pH 4 and 10), and, more importantly, reusability (∼50% activity after 8 repetitive cycles of usage). Enzyme kinetics showed an increase in the Vmax (from 35.76 to 51.14μM/min) and Kcat (from 365s(-1) to 520s(-1)) after immobilization. The superior catalytic properties of immobilized EstH suggest its great potential in biotechnology and industrial processes.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Rahman MA,Culsum U,Kumar A,Gao H,Hu N

doi

10.1016/j.ijbiomac.2016.03.016

subject

Has Abstract

pub_date

2016-06-01 00:00:00

pages

488-97

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(16)30240-9

journal_volume

87

pub_type

杂志文章

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